Evidence map›Paper›PMID 29242355›Full record

ArticleMolecular pharmacology2018

The Bioactive Protein-Ligand Conformation of GluN2C-Selective Positive Allosteric Modulators Bound to the NMDA Receptor.

Thomas M Kaiser, Steven A Kell, Hirofumi Kusumoto, Gil Shaulsky, Subhrajit Bhattacharya, Matthew P Epplin, Katie L Strong, Eric J Miller, Bryan D Cox, David S Menaldino and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular pharmacology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.4field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Biological chemistry · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 1 institution in 1 country.

Thomas M KaiserDepartment of Chemistry, Emory University, Atlanta, Georgia (T.M.K., S.A.K., M.P.E., K.L.S., E.J.M., B.D.C., D.S.M., D.C.L., P.B.B.); and Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia (H.K., G.S., S.B., S.F.T.).
Steven A KellDepartment of Chemistry, Emory University, Atlanta, Georgia (T.M.K., S.A.K., M.P.E., K.L.S., E.J.M., B.D.C., D.S.M., D.C.L., P.B.B.); and Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia (H.K., G.S., S.B., S.F.T.).
Hirofumi KusumotoDepartment of Chemistry, Emory University, Atlanta, Georgia (T.M.K., S.A.K., M.P.E., K.L.S., E.J.M., B.D.C., D.S.M., D.C.L., P.B.B.); and Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia (H.K., G.S., S.B., S.F.T.).
Gil ShaulskyDepartment of Chemistry, Emory University, Atlanta, Georgia (T.M.K., S.A.K., M.P.E., K.L.S., E.J.M., B.D.C., D.S.M., D.C.L., P.B.B.); and Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia (H.K., G.S., S.B., S.F.T.).
Subhrajit BhattacharyaDepartment of Chemistry, Emory University, Atlanta, Georgia (T.M.K., S.A.K., M.P.E., K.L.S., E.J.M., B.D.C., D.S.M., D.C.L., P.B.B.); and Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia (H.K., G.S., S.B., S.F.T.).
Matthew P EpplinDepartment of Chemistry, Emory University, Atlanta, Georgia (T.M.K., S.A.K., M.P.E., K.L.S., E.J.M., B.D.C., D.S.M., D.C.L., P.B.B.); and Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia (H.K., G.S., S.B., S.F.T.).
Katie L StrongDepartment of Chemistry, Emory University, Atlanta, Georgia (T.M.K., S.A.K., M.P.E., K.L.S., E.J.M., B.D.C., D.S.M., D.C.L., P.B.B.); and Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia (H.K., G.S., S.B., S.F.T.).
Eric J MillerDepartment of Chemistry, Emory University, Atlanta, Georgia (T.M.K., S.A.K., M.P.E., K.L.S., E.J.M., B.D.C., D.S.M., D.C.L., P.B.B.); and Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia (H.K., G.S., S.B., S.F.T.).
Bryan D CoxDepartment of Chemistry, Emory University, Atlanta, Georgia (T.M.K., S.A.K., M.P.E., K.L.S., E.J.M., B.D.C., D.S.M., D.C.L., P.B.B.); and Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia (H.K., G.S., S.B., S.F.T.).
David S MenaldinoDepartment of Chemistry, Emory University, Atlanta, Georgia (T.M.K., S.A.K., M.P.E., K.L.S., E.J.M., B.D.C., D.S.M., D.C.L., P.B.B.); and Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia (H.K., G.S., S.B., S.F.T.).
Dennis C LiottaDepartment of Chemistry, Emory University, Atlanta, Georgia (T.M.K., S.A.K., M.P.E., K.L.S., E.J.M., B.D.C., D.S.M., D.C.L., P.B.B.); and Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia (H.K., G.S., S.B., S.F.T.).
Stephen F TraynelisDepartment of Chemistry, Emory University, Atlanta, Georgia (T.M.K., S.A.K., M.P.E., K.L.S., E.J.M., B.D.C., D.S.M., D.C.L., P.B.B.); and Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia (H.K., G.S., S.B., S.F.T.) pburger@emory.edu strayne@emory.edu.
Pieter B BurgerDepartment of Chemistry, Emory University, Atlanta, Georgia (T.M.K., S.A.K., M.P.E., K.L.S., E.J.M., B.D.C., D.S.M., D.C.L., P.B.B.); and Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia (H.K., G.S., S.B., S.F.T.) pburger@emory.edu strayne@emory.edu.
Emory University · US

Funding

Control of Glutamate Receptor FunctionR01NS036654 · NINDS · EMORY UNIVERSITY · PI TRAYNELIS, STEPHEN F · 1998 to 2018
$3.7M
Mechanism of Action of Novel Subunit-Selective NMDA Receptor ModulatorsR01NS065371 · NINDS · EMORY UNIVERSITY · PI TRAYNELIS, STEPHEN F · 2009 to 2018
$3.4M
Control of glutamate receptor functionR37NS036654 · NINDS · EMORY UNIVERSITY · PI TRAYNELIS, STEPHEN F · 2007 to 2013
$2.4M
NINDS NIH HHS R01 NS036654NINDS NIH HHS R01 NS065371NINDS NIH HHS R37 NS036654
6 · The paper itself

Abstract

PubMed holds no abstract for this paper.

Indexed as

Allosteric RegulationAnimalsBinding SitesExcitatory Amino Acid AgentsLigandsMagnetic Resonance SpectroscopyModels, MolecularMolecular Dynamics SimulationPatch-Clamp TechniquesProtein ConformationProton Magnetic Resonance SpectroscopyReceptors, N-Methyl-D-AspartateReproducibility of ResultsStereoisomerismXenopus laevisExcitatory Amino Acid AgentsLigandsNR2C NMDA receptorReceptors, N-Methyl-D-Aspartate

Identifiers

PMID29242355
PMCPMC5767683
OpenAlexW2771915833

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.